Time of initiation of the barley endosperm response to gibberellin A3, gibberellin A14 and kaurene

Summary Gibberellin A₁₄ and kaurene, precursors of gibberellin A₃, are active in the barley endosperm reducing-sugar assay, but require longer incubation periods for activity to be observed than does GA₃. This finding shows that the incubation period must be considered when determining whether a compound is active in this assay. The longer incubation periods required by GA₁₄ and kaurene may reflect reduced rates of penetration, or reduced activity within the cell, or the time required for conversion to a physiologically active form.     

Golgi apparatus mediated polysaccharide secretion by outer root cap cells of Zea mays

Summary In the outer cap cells of roots of Zea mays, secretion is accompanied by hypertrophy of dictyosome cisternae with formation of large secretory vesicles. Vesicle contents are subsequently released from the protoplast by fusion of the vesicle membrane with the plasma membrane. The secreted material, a highly hydrated polysaccharide, was localized intracellularly by the periodic acid-Schiff reaction. Under appropriate conditions, the product moves outward through the cell wall after discharge from the protoplast, and appears as a droplet adhering to the root tip. Under conditions where the secretory product accumulates at the inner wall surfaces, no external droplet is formed.The secretory activity has an active phase that is sensitive to metabolic inhibitors and influenced by temperature (Q₁₀>2), and a passive phase that is independent of temperature, insensitive to metabolic inhibitors but sensitive to osmotic agents. The active phase is characterized by a temperature-independent periodicity (3 hours). Sucrose supplied to the growth medium increases the amount of polysaccharide secreted. Polysaccharide synthesis, segregation into vesicles, and discharge from the protoplast are assumed to require active metabolism; the step involving extrusion of polysaccharide through the cell wall region appears to be a passive process influenced by the degree of hydration of the polysaccharide and by cell turgor.Purdue University Agricultural Experiment Station Journal Paper No. 2967; Charles F. Kettering Research Laboratory Contribution No. 261.     

Properties of substituted 2-trifluoromethylbenzimidazoles as uncouplers of oxidative phosphorylation

1. The activity of 25 substituted 2-trifluoromethylbenzimidazoles in uncoupling oxidative phosphorylation by rat-liver mitochondria has been compared. 2. For halogen- or mixed-halogen- and alkyl-substituted analogues, uncoupling activity was proportional to the acidity of the imidazole -NH group. Tetrachloro-2-trifluoromethylbenzimidazole was the most active (50% uncoupling of oxidative phosphorylation at 7.9x10(-8)m, pK5.04). Nitro-substituted analogues were less active than predicted from pK considerations or from partition-coefficient measurements. 3. Introduction of an -NH(2) or -CO(2)H substitutent caused a loss of uncoupling activity, as did alkylation at position 1 of the imidazole ring. 4. Benzimidazoles active as uncouplers stimulated mitochondrial adenosine triphosphatase but not all stimulated the oxidation of succinate in the absence of a phosphate acceptor. 5. 4,5-Dichloro-2-trifluoromethylbenzimidazole inhibited the succinate-oxidase system at about the same concentration required for uncoupling (0.52mum for 50% inhibition of both activities) and the site of this inhibition appears to lie between succinate dehydrogenase and cytochrome b.